HEADER OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 25-MAR-80 2SOD
TITLE DETERMINATION AND ANALYSIS OF THE 2 ANGSTROM STRUCTURE OF COPPER, ZINC
TITLE 2 SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER,ZINC SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: O, Y, B, G;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.TAINER,E.D.GETZOFF,J.S.RICHARDSON,D.C.RICHARDSON
REVDAT 12 27-SEP-23 2SOD 1 REMARK LINK
REVDAT 11 13-JUL-11 2SOD 1 VERSN
REVDAT 10 24-FEB-09 2SOD 1 VERSN
REVDAT 9 01-APR-03 2SOD 1 JRNL
REVDAT 8 15-JAN-91 2SOD 1 HET
REVDAT 7 31-JAN-84 2SOD 1 REMARK
REVDAT 6 06-DEC-83 2SOD 1 REMARK
REVDAT 5 30-SEP-83 2SOD 1 REVDAT
REVDAT 4 25-OCT-82 2SOD 1 JRNL
REVDAT 3 20-APR-81 2SOD 1 SHEET
REVDAT 2 31-DEC-80 2SOD 1 REMARK
REVDAT 1 07-MAY-80 2SOD 0
SPRSDE 07-MAY-80 2SOD 1SOD
JRNL AUTH J.A.TAINER,E.D.GETZOFF,K.M.BEEM,J.S.RICHARDSON,
JRNL AUTH 2 D.C.RICHARDSON
JRNL TITL DETERMINATION AND ANALYSIS OF THE 2 A-STRUCTURE OF COPPER,
JRNL TITL 2 ZINC SUPEROXIDE DISMUTASE.
JRNL REF J.MOL.BIOL. V. 160 181 1982
JRNL REFN ISSN 0022-2836
JRNL PMID 7175933
JRNL DOI 10.1016/0022-2836(82)90174-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.TAINER,E.D.GETZOFF,J.S.RICHARDSON,D.C.RICHARDSON
REMARK 1 TITL STRUCTURE AND MECHANISM OF COPPER, ZINC SUPEROXIDE DISMUTASE
REMARK 1 REF NATURE V. 306 284 1983
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.D.GETZOFF,J.A.TAINER,P.K.WEINER,P.A.KOLLMAN,
REMARK 1 AUTH 2 J.S.RICHARDSON,D.C.RICHARDSON
REMARK 1 TITL ELECTROSTATIC RECOGNITION BETWEEN SUPEROXIDE AND COPPER,
REMARK 1 TITL 2 ZINC SUPEROXIDE DISMUTASE
REMARK 1 REF NATURE V. 306 287 1983
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.M.BEEM,D.C.RICHARDSON,K.V.RAJAGOPALAN
REMARK 1 TITL METAL SITES OF COPPER-ZINC SUPEROXIDE DISMUTASE
REMARK 1 REF BIOCHEMISTRY V. 16 1930 1977
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.S.RICHARDSON,D.C.RICHARDSON,K.A.THOMAS,E.W.SILVERTON,
REMARK 1 AUTH 2 D.R.DAVIES
REMARK 1 TITL SIMILARITY OF THREE-DIMENSIONAL STRUCTURE BETWEEN THE
REMARK 1 TITL 2 IMMUNOGLOBULIN DOMAIN AND THE COPPER,ZINC SUPEROXIDE
REMARK 1 TITL 3 DISMUTASE SUBUNIT
REMARK 1 REF J.MOL.BIOL. V. 102 221 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.S.RICHARDSON,R.A.THOMAS,D.C.RICHARDSON
REMARK 1 TITL ALPHA-CARBON COORDINATES FOR BOVINE CU,ZN SUPEROXIDE
REMARK 1 TITL 2 DISMUTASE
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 63 986 1975
REMARK 1 REFN ISSN 0006-291X
REMARK 1 REFERENCE 6
REMARK 1 AUTH J.S.RICHARDSON,K.A.THOMAS,B.H.RUBIN,D.C.RICHARDSON
REMARK 1 TITL CRYSTAL STRUCTURE OF BOVINE CU,ZN SUPEROXIDE DISMUTASE AT 3
REMARK 1 TITL 2 ANGSTROMS RESOLUTION,CHAIN TRACING AND METAL LIGANDS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 72 1349 1975
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 7
REMARK 1 AUTH K.A.THOMAS,B.H.RUBIN,C.J.BIER,J.S.RICHARDSON,D.C.RICHARDSON
REMARK 1 TITL THE CRYSTAL STRUCTURE OF BOVINE CU2+,ZN2+ SUPEROXIDE
REMARK 1 TITL 2 DISMUTASE AT 5.5 ANGSTROMS RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 249 5677 1974
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 8
REMARK 1 AUTH D.C.RICHARDSON,C.J.BIER,J.S.RICHARDSON
REMARK 1 TITL TWO CRYSTAL FORMS OF BOVINE SUPEROXIDE DISMUTASE
REMARK 1 REF J.BIOL.CHEM. V. 247 6368 1972
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.256
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 COORDINATES IN THE A*BC ORTHOGONAL FRAME ARE PRESENTED
REMARK 3 BELOW FOR FOUR MONOMERS. ONE ENZYMATICALLY ACTIVE SOD
REMARK 3 DIMER COMPRISES MONOMERS ORANGE (CHAIN INDICATOR O) AND
REMARK 3 YELLOW (Y). ANOTHER DIMER COMPRISES MONOMERS BLUE (B) AND
REMARK 3 GREEN (G).
REMARK 3
REMARK 3 ONLY THOSE HYDROGEN BONDS OF WHICH THE DEPOSITORS ARE
REMARK 3 MOST CERTAIN ARE PRESENTED ON THE CONECT RECORDS BELOW.
REMARK 4
REMARK 4 2SOD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.64179
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.16304
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 -4.16391
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.64179
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.16304
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 -4.16391
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE TRANSFORMATION WHICH WILL PLACE THE YELLOW MONOMER INTO
REMARK 300 BEST ALIGNMENT WITH THE ORANGE MONOMER IS GIVEN BY MTRIX 1
REMARK 300 BELOW. THE TRANSFORMATION WHICH WILL PLACE THE BLUE
REMARK 300 MONOMER INTO BEST ALIGNMENT WITH THE ORANGE MONOMER IS
REMARK 300 GIVEN BY MTRIX 2 BELOW. THE TRANSFORMATION WHICH WILL
REMARK 300 PLACE THE GREEN MONOMER INTO BEST ALIGNMENT WITH THE
REMARK 300 ORANGE MONOMER IS GIVEN BY MTRIX 3 BELOW.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, Y
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU O 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 44 ND1
REMARK 620 2 HIS O 46 NE2 130.2
REMARK 620 3 HIS O 61 NE2 74.7 89.1
REMARK 620 4 HIS O 118 NE2 93.7 106.4 164.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN O 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 61 ND1
REMARK 620 2 HIS O 69 ND1 111.1
REMARK 620 3 HIS O 78 ND1 107.5 130.0
REMARK 620 4 ASP O 81 OD1 100.0 78.7 124.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU Y 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Y 44 ND1
REMARK 620 2 HIS Y 46 NE2 137.0
REMARK 620 3 HIS Y 61 NE2 78.7 87.0
REMARK 620 4 HIS Y 118 NE2 91.2 109.9 162.4
REMARK 620 5 HOH Y 154 O 119.3 95.9 76.8 96.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Y 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Y 61 ND1
REMARK 620 2 HIS Y 69 ND1 110.8
REMARK 620 3 HIS Y 78 ND1 109.6 119.7
REMARK 620 4 ASP Y 81 OD1 114.2 104.9 97.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 44 ND1
REMARK 620 2 HIS B 46 NE2 140.3
REMARK 620 3 HIS B 61 NE2 81.9 91.6
REMARK 620 4 HIS B 118 NE2 99.4 104.6 150.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 61 ND1
REMARK 620 2 HIS B 69 ND1 105.4
REMARK 620 3 HIS B 78 ND1 117.9 122.4
REMARK 620 4 ASP B 81 OD1 99.6 91.3 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU G 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 44 ND1
REMARK 620 2 HIS G 46 NE2 149.9
REMARK 620 3 HIS G 61 NE2 87.3 98.8
REMARK 620 4 HIS G 118 NE2 84.4 104.5 146.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 61 ND1
REMARK 620 2 HIS G 69 ND1 109.2
REMARK 620 3 HIS G 78 ND1 121.3 116.4
REMARK 620 4 ASP G 81 OD1 105.8 90.1 109.0
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 EACH MONOMER CONTAINS AN ACETYL GROUP BLOCKING THE
REMARK 700 N-TERMINUS, 151 RESIDUES, ZN ION, CU ION AND A WATER
REMARK 700 MOLECULE. THE DOMINANT STRUCTURAL FEATURE OF EACH MONOMER
REMARK 700 IS AN EIGHT-STRANDED ANTI-PARALLEL BETA-BARREL. THERE ARE,
REMARK 700 HOWEVER, NO HYDROGEN BONDS BETWEEN STRANDS 4 AND 5. THIS
REMARK 700 BARREL IS DESCRIBED IN SHEET RECORDS BELOW AS A
REMARK 700 NINE-STRANDED SHEET WITH IDENTICAL FIRST AND LAST STRANDS.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CUO
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: COPPER BINDING SITE AND THE ENZYMATICALLY ACTIVE
REMARK 800 SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNO
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CUY
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: COPPER BINDING SITE AND THE ENZYMATICALLY ACTIVE
REMARK 800 SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNY
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CUB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: COPPER BINDING SITE AND THE ENZYMATICALLY ACTIVE
REMARK 800 SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CUG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: COPPER BINDING SITE AND THE ENZYMATICALLY ACTIVE
REMARK 800 SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU O 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN O 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU Y 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Y 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 153
DBREF 2SOD O 1 151 UNP P00442 SODC_BOVIN 1 151
DBREF 2SOD Y 1 151 UNP P00442 SODC_BOVIN 1 151
DBREF 2SOD B 1 151 UNP P00442 SODC_BOVIN 1 151
DBREF 2SOD G 1 151 UNP P00442 SODC_BOVIN 1 151
SEQRES 1 O 152 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 O 152 PRO VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP
SEQRES 3 O 152 THR VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU
SEQRES 4 O 152 GLY ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN
SEQRES 5 O 152 THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO
SEQRES 6 O 152 LEU SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG
SEQRES 7 O 152 HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN
SEQRES 8 O 152 GLY VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER
SEQRES 9 O 152 LEU SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL
SEQRES 10 O 152 VAL HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN
SEQRES 11 O 152 GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU
SEQRES 12 O 152 ALA CYS GLY VAL ILE GLY ILE ALA LYS
SEQRES 1 Y 152 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 Y 152 PRO VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP
SEQRES 3 Y 152 THR VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU
SEQRES 4 Y 152 GLY ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN
SEQRES 5 Y 152 THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO
SEQRES 6 Y 152 LEU SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG
SEQRES 7 Y 152 HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN
SEQRES 8 Y 152 GLY VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER
SEQRES 9 Y 152 LEU SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL
SEQRES 10 Y 152 VAL HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN
SEQRES 11 Y 152 GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU
SEQRES 12 Y 152 ALA CYS GLY VAL ILE GLY ILE ALA LYS
SEQRES 1 B 152 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 B 152 PRO VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP
SEQRES 3 B 152 THR VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU
SEQRES 4 B 152 GLY ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN
SEQRES 5 B 152 THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO
SEQRES 6 B 152 LEU SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG
SEQRES 7 B 152 HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN
SEQRES 8 B 152 GLY VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER
SEQRES 9 B 152 LEU SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL
SEQRES 10 B 152 VAL HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN
SEQRES 11 B 152 GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU
SEQRES 12 B 152 ALA CYS GLY VAL ILE GLY ILE ALA LYS
SEQRES 1 G 152 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 G 152 PRO VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP
SEQRES 3 G 152 THR VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU
SEQRES 4 G 152 GLY ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN
SEQRES 5 G 152 THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO
SEQRES 6 G 152 LEU SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG
SEQRES 7 G 152 HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN
SEQRES 8 G 152 GLY VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER
SEQRES 9 G 152 LEU SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL
SEQRES 10 G 152 VAL HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN
SEQRES 11 G 152 GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU
SEQRES 12 G 152 ALA CYS GLY VAL ILE GLY ILE ALA LYS
HET ACE O 0 3
HET ACE Y 0 3
HET ACE B 0 3
HET ACE G 0 3
HET CU O 152 1
HET ZN O 153 1
HET CU Y 152 1
HET ZN Y 153 1
HET CU B 152 1
HET ZN B 153 1
HET CU G 152 1
HET ZN G 153 1
HETNAM ACE ACETYL GROUP
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
FORMUL 1 ACE 4(C2 H4 O)
FORMUL 5 CU 4(CU 2+)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 13 HOH *4(H2 O)
HELIX 1 H1O GLU O 131 THR O 135 1VERY POOR SNGL LOOP ALPH-HELX 5
HELIX 2 H1Y GLU Y 131 THR Y 135 1VERY POOR SNGL LOOP ALPH-HELX 5
HELIX 3 H1B GLU B 131 THR B 135 1VERY POOR SNGL LOOP ALPH-HELX 5
HELIX 4 H1G GLU G 131 THR G 135 1VERY POOR SNGL LOOP ALPH-HELX 5
SHEET 1 S1O 9 ALA O 4 LYS O 9 0
SHEET 2 S1O 9 GLN O 15 GLU O 21 -1 N ALA O 4 O PHE O 20
SHEET 3 S1O 9 VAL O 27 THR O 34 -1 N GLU O 21 O VAL O 28
SHEET 4 S1O 9 ALA O 93 ASP O 99 -1 N VAL O 29 O ILE O 97
SHEET 5 S1O 9 GLY O 80 ALA O 87 -1
SHEET 6 S1O 9 GLY O 39 HIS O 46 -1 N VAL O 85 O HIS O 41
SHEET 7 S1O 9 ARG O 113 HIS O 118 -1 N HIS O 44 O VAL O 116
SHEET 8 S1O 9 CYS O 144 GLY O 148 -1 N MET O 115 O GLY O 145
SHEET 9 S1O 9 ALA O 4 LYS O 9 -1 N VAL O 146 O VAL O 7
SHEET 1 S1Y 9 ALA Y 4 LYS Y 9 0
SHEET 2 S1Y 9 GLN Y 15 GLU Y 21 -1 N ALA Y 4 O PHE Y 20
SHEET 3 S1Y 9 VAL Y 27 THR Y 34 -1 N GLU Y 21 O VAL Y 28
SHEET 4 S1Y 9 ALA Y 93 ASP Y 99 -1 N VAL Y 29 O ILE Y 97
SHEET 5 S1Y 9 GLY Y 80 ALA Y 87 -1
SHEET 6 S1Y 9 GLY Y 39 HIS Y 46 -1 N VAL Y 85 O HIS Y 41
SHEET 7 S1Y 9 ARG Y 113 HIS Y 118 -1 N HIS Y 44 O VAL Y 116
SHEET 8 S1Y 9 CYS Y 144 GLY Y 148 -1 N MET Y 115 O GLY Y 145
SHEET 9 S1Y 9 ALA Y 4 LYS Y 9 -1 N VAL Y 146 O VAL Y 7
SHEET 1 S1B 9 ALA B 4 LYS B 9 0
SHEET 2 S1B 9 GLN B 15 GLU B 21 -1 N ALA B 4 O PHE B 20
SHEET 3 S1B 9 VAL B 27 THR B 34 -1 N GLU B 21 O VAL B 28
SHEET 4 S1B 9 ALA B 93 ASP B 99 -1 N VAL B 29 O ILE B 97
SHEET 5 S1B 9 GLY B 80 ALA B 87 -1
SHEET 6 S1B 9 GLY B 39 HIS B 46 -1 N VAL B 85 O HIS B 41
SHEET 7 S1B 9 ARG B 113 HIS B 118 -1 N HIS B 44 O VAL B 116
SHEET 8 S1B 9 CYS B 144 GLY B 148 -1 N MET B 115 O GLY B 145
SHEET 9 S1B 9 ALA B 4 LYS B 9 -1 N VAL B 146 O VAL B 7
SHEET 1 S1G 9 ALA G 4 LYS G 9 0
SHEET 2 S1G 9 GLN G 15 GLU G 21 -1 N ALA G 4 O PHE G 20
SHEET 3 S1G 9 VAL G 27 THR G 34 -1 N GLU G 21 O VAL G 28
SHEET 4 S1G 9 ALA G 93 ASP G 99 -1 N VAL G 29 O ILE G 97
SHEET 5 S1G 9 GLY G 80 ALA G 87 -1
SHEET 6 S1G 9 GLY G 39 HIS G 46 -1 N VAL G 85 O HIS G 41
SHEET 7 S1G 9 ARG G 113 HIS G 118 -1 N HIS G 44 O VAL G 116
SHEET 8 S1G 9 CYS G 144 GLY G 148 -1 N MET G 115 O GLY G 145
SHEET 9 S1G 9 ALA G 4 LYS G 9 -1 N VAL G 146 O VAL G 7
SSBOND 1 CYS O 55 CYS O 144 1555 1555 1.98
SSBOND 2 CYS Y 55 CYS Y 144 1555 1555 1.97
SSBOND 3 CYS B 55 CYS B 144 1555 1555 2.07
SSBOND 4 CYS G 55 CYS G 144 1555 1555 2.00
LINK C ACE O 0 N ALA O 1 1555 1555 1.33
LINK C ACE Y 0 N ALA Y 1 1555 1555 1.39
LINK C ACE B 0 N ALA B 1 1555 1555 1.36
LINK C ACE G 0 N ALA G 1 1555 1555 1.31
LINK ND1 HIS O 44 CU CU O 152 1555 1555 2.01
LINK NE2 HIS O 46 CU CU O 152 1555 1555 2.11
LINK NE2 HIS O 61 CU CU O 152 1555 1555 2.21
LINK ND1 HIS O 61 ZN ZN O 153 1555 1555 2.10
LINK ND1 HIS O 69 ZN ZN O 153 1555 1555 2.14
LINK ND1 HIS O 78 ZN ZN O 153 1555 1555 2.04
LINK OD1 ASP O 81 ZN ZN O 153 1555 1555 1.91
LINK NE2 HIS O 118 CU CU O 152 1555 1555 2.10
LINK ND1 HIS Y 44 CU CU Y 152 1555 1555 1.96
LINK NE2 HIS Y 46 CU CU Y 152 1555 1555 2.12
LINK NE2 HIS Y 61 CU CU Y 152 1555 1555 1.98
LINK ND1 HIS Y 61 ZN ZN Y 153 1555 1555 2.07
LINK ND1 HIS Y 69 ZN ZN Y 153 1555 1555 2.08
LINK ND1 HIS Y 78 ZN ZN Y 153 1555 1555 2.16
LINK OD1 ASP Y 81 ZN ZN Y 153 1555 1555 2.07
LINK NE2 HIS Y 118 CU CU Y 152 1555 1555 1.99
LINK CU CU Y 152 O HOH Y 154 1555 1555 2.49
LINK ND1 HIS B 44 CU CU B 152 1555 1555 2.00
LINK NE2 HIS B 46 CU CU B 152 1555 1555 2.15
LINK NE2 HIS B 61 CU CU B 152 1555 1555 2.26
LINK ND1 HIS B 61 ZN ZN B 153 1555 1555 2.07
LINK ND1 HIS B 69 ZN ZN B 153 1555 1555 2.12
LINK ND1 HIS B 78 ZN ZN B 153 1555 1555 2.04
LINK OD1 ASP B 81 ZN ZN B 153 1555 1555 2.00
LINK NE2 HIS B 118 CU CU B 152 1555 1555 1.98
LINK ND1 HIS G 44 CU CU G 152 1555 1555 2.06
LINK NE2 HIS G 46 CU CU G 152 1555 1555 2.02
LINK NE2 HIS G 61 CU CU G 152 1555 1555 2.21
LINK ND1 HIS G 61 ZN ZN G 153 1555 1555 2.08
LINK ND1 HIS G 69 ZN ZN G 153 1555 1555 2.13
LINK ND1 HIS G 78 ZN ZN G 153 1555 1555 2.09
LINK OD1 ASP G 81 ZN ZN G 153 1555 1555 1.99
LINK NE2 HIS G 118 CU CU G 152 1555 1555 2.07
SITE 1 CUO 4 HIS O 44 HIS O 46 HIS O 61 HIS O 118
SITE 1 ZNO 4 HIS O 61 HIS O 69 HIS O 78 ASP O 81
SITE 1 CUY 4 HIS Y 44 HIS Y 46 HIS Y 61 HIS Y 118
SITE 1 ZNY 4 HIS Y 61 HIS Y 69 HIS Y 78 ASP Y 81
SITE 1 CUB 4 HIS B 44 HIS B 46 HIS B 61 HIS B 118
SITE 1 ZNB 4 HIS B 61 HIS B 69 HIS B 78 ASP B 81
SITE 1 CUG 4 HIS G 44 HIS G 46 HIS G 61 HIS G 118
SITE 1 ZNG 4 HIS G 61 HIS G 69 HIS G 78 ASP G 81
SITE 1 AC1 4 HIS O 44 HIS O 46 HIS O 61 HIS O 118
SITE 1 AC2 4 HIS O 61 HIS O 69 HIS O 78 ASP O 81
SITE 1 AC3 5 HIS Y 44 HIS Y 46 HIS Y 61 HIS Y 118
SITE 2 AC3 5 HOH Y 154
SITE 1 AC4 4 HIS Y 61 HIS Y 69 HIS Y 78 ASP Y 81
SITE 1 AC5 4 HIS B 44 HIS B 46 HIS B 61 HIS B 118
SITE 1 AC6 4 HIS B 61 HIS B 69 HIS B 78 ASP B 81
SITE 1 AC7 4 HIS G 44 HIS G 46 HIS G 61 HIS G 118
SITE 1 AC8 4 HIS G 61 HIS G 69 HIS G 78 ASP G 81
CRYST1 93.650 90.330 71.650 90.00 95.10 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010720 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011071 0.000000 0.00000
SCALE3 0.001246 0.000000 0.013957 0.00000
MTRIX1 1 -0.781140 0.204080 -0.590060 -59.69421 1
MTRIX2 1 0.162190 -0.846300 -0.507420 29.26225 1
MTRIX3 1 -0.602920 -0.492070 0.627980 -12.96087 1
MTRIX1 2 -0.766640 -0.067560 0.638520 -53.22701 1
MTRIX2 2 0.203310 0.917740 0.341210 -0.63586 1
MTRIX3 2 -0.609040 0.391400 -0.689830 -21.95514 1
MTRIX1 3 0.992260 -0.016400 -0.123090 -2.98838 1
MTRIX2 3 0.003860 -0.986680 0.162630 32.25722 1
MTRIX3 3 -0.124120 -0.161850 -0.978980 3.34240 1
HETATM 1 C ACE O 0 -21.225 25.808 -21.169 1.00 19.00 C
HETATM 2 O ACE O 0 -20.735 26.891 -20.713 1.00 19.08 O
HETATM 3 CH3 ACE O 0 -22.681 25.631 -21.581 1.00 18.60 C
(ATOM LINES ARE NOT SHOWN.)
END
